ID A2RJT4_LACLM Unreviewed; 359 AA.
AC A2RJT4;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Putative glycerol dehydrogenase {ECO:0000313|EMBL:CAL97539.1};
DE EC=1.1.-.- {ECO:0000313|EMBL:CAL97539.1};
GN OrderedLocusNames=llmg_0945 {ECO:0000313|EMBL:CAL97539.1};
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870 {ECO:0000313|EMBL:CAL97539.1, ECO:0000313|Proteomes:UP000000364};
RN [1] {ECO:0000313|EMBL:CAL97539.1, ECO:0000313|Proteomes:UP000000364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363 {ECO:0000313|EMBL:CAL97539.1,
RC ECO:0000313|Proteomes:UP000000364};
RX PubMed=17307855; DOI=10.1128/JB.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000112-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000112-1};
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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DR EMBL; AM406671; CAL97539.1; -; Genomic_DNA.
DR RefSeq; WP_011834889.1; NZ_WJVF01000006.1.
DR AlphaFoldDB; A2RJT4; -.
DR SMR; A2RJT4; -.
DR STRING; 416870.llmg_0945; -.
DR KEGG; llm:llmg_0945; -.
DR eggNOG; COG0371; Bacteria.
DR HOGENOM; CLU_044754_2_0_9; -.
DR OrthoDB; 5198708at2; -.
DR PhylomeDB; A2RJT4; -.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR CDD; cd08172; GlyDH-like; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; GLYCEROL DEHYDROGENASE; 1.
DR PANTHER; PTHR43616:SF3; HYDROXYCARBOXYLATE DEHYDROGENASE A; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000112-1}; NAD {ECO:0000256|PIRSR:PIRSR000112-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAL97539.1}; Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT DOMAIN 12..331
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT BINDING 89..93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 111..114
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 166
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 252
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 269
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 359 AA; 39583 MW; 093884312AE6DFFC CRC64;
MKLSEEVRPG ANRYVSGQEI LQDLEAYLAP FKELAVITGE KSFQVFQDFY PKTLSYPIFH
YDGTASVENG KKLAKEIGNV EAILAIGGGR LIDTCKVVAQ ELDCELIIIP TLVSNCAPYT
PVAALYHPDH TFDKVGYLNK VSYLTLVDYD FLVATPYDYF VAGIGDTLAK WYEMEGIIRQ
VPQEELSASV RLGFVSAKEI FKILFADSKA ALEDLSKQKV SPAFGRIVDT IIELSGTVGG
FAGTYGRMSG AHALHNGLSL CPETHAILHG SKVAYGVLVQ LAYTRDYLEI EKLLPFYREN
HLPASLEEIN LSNPNLKKLK EAAEFAASPV ESYRLIDEKV SGEKIISAIK VLESLVSKK
//
